{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["20(15)"],"submitter":["Stegh AH"],"pubmed_abstract":["Caspase 8 plays an essential role in the execution of death receptor-mediated apoptosis. To determine the localization of endogenous caspase 8, we used a panel of subunit-specific anti-caspase 8 monoclonal antibodies in confocal immunofluorescence microscopy. In the human breast carcinoma cell line MCF7, caspase 8 predominantly colocalized with and bound to mitochondria. After induction of apoptosis through CD95 or tumor necrosis factor receptor I, active caspase 8 translocated to plectin, a major cross-linking protein of the three main cytoplasmic filament systems, whereas the caspase 8 prodomain remained bound to mitochondria. Plectin was quantitatively cleaved by caspase 8 at Asp 2395 in the center of the molecule in all cells tested. Cleavage of plectin clearly preceded that of other c"],"journal":["Molecular and cellular biology"],"pagination":["5665-79"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC86037"],"repository":["biostudies-literature"],"pubmed_title":["Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosis."],"pmcid":["PMC86037"],"pubmed_authors":["Seper M","Andra K","Peter ME","Herrmann H","Stegh AH","Wiche G","Krammer PH","Lampel S","Weisenberger D"],"additional_accession":[]},"is_claimable":false,"name":"Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosis.","description":"Caspase 8 plays an essential role in the execution of death receptor-mediated apoptosis. To determine the localization of endogenous caspase 8, we used a panel of subunit-specific anti-caspase 8 monoclonal antibodies in confocal immunofluorescence microscopy. In the human breast carcinoma cell line MCF7, caspase 8 predominantly colocalized with and bound to mitochondria. After induction of apoptosis through CD95 or tumor necrosis factor receptor I, active caspase 8 translocated to plectin, a major cross-linking protein of the three main cytoplasmic filament systems, whereas the caspase 8 prodomain remained bound to mitochondria. Plectin was quantitatively cleaved by caspase 8 at Asp 2395 in the center of the molecule in all cells tested. Cleavage of plectin clearly preceded that of other c","dates":{"release":"2000-01-01T00:00:00Z","publication":"2000 Aug","modification":"2025-04-05T10:13:52.011Z","creation":"2019-03-27T00:18:20Z"},"accession":"S-EPMC86037","cross_references":{"pubmed":["10891503"],"doi":["10.1128/MCB.20.15.5665-5679.2000"]}}